Crystal structure of the protease-resistant core domain of Yersinia pestis virulence factor YopR.
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ABSTRACT:
SUBMITTER: Schubot FD
PROVIDER: S-EPMC2253397 | biostudies-literature | 2005 Jun
REPOSITORIES: biostudies-literature
Publications
Crystal structure of the protease-resistant core domain of Yersinia pestis virulence factor YopR.
Schubot Florian D FD Cherry Scott S Austin Brian P BP Tropea Joseph E JE Waugh David S DS
Protein science : a publication of the Protein Society 20050601 6
Yersinia pestis, the causative agent of the plague, employs a type III secretion system (T3SS) to secrete and translocate virulence factors into to the cytoplasm of mammalian host cells. One of the secreted virulence factors is YopR. Little is known about the function of YopR other than that it is secreted into the extracellular milieu during the early stages of infection and that it contributes to virulence. Hoping to gain some insight into the function of YopR, we determined the crystal struct ...[more]
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